Tag | Content |
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CPLM ID | CPLM-021092 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aconitate hydratase, mitochondrial |
Protein Synonyms/Alias | Aconitase; Citrate hydro-lyase |
Gene Name | Aco2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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50 | IRYDLLEKNINIVRK | acetylation | [1] | 68 | RPLTLSEKIVYGHLD | acetylation | [1] | 86 | NQEIERGKTYLRLRP | acetylation | [1] | 138 | EAQLGGEKDLRRAKD | acetylation | [1] | 144 | EKDLRRAKDINQEVY | acetylation | [1] | 228 | PWELKCPKVIGVKLT | acetylation | [1] | 233 | CPKVIGVKLTGTLSG | acetylation | [1] | 245 | LSGWTSPKDVILKVA | acetylation | [1] | 304 | FPYNHRMKKYLSKTG | acetylation | [1] | 305 | PYNHRMKKYLSKTGR | acetylation | [1] | 309 | RMKKYLSKTGRADIA | acetylation | [1] | 401 | GRSAAVAKQALAHGL | acetylation | [1] | 462 | WDRKDIKKGEKNTIV | acetylation | [1] | 517 | ETDFLTGKDGKKFKL | acetylation | [1] | 520 | FLTGKDGKKFKLEAP | acetylation | [1] | 521 | LTGKDGKKFKLEAPD | acetylation | [1] | 523 | GKDGKKFKLEAPDAD | acetylation | [1] | 549 | DTYQHPPKDSSGQRV | acetylation | [1] | 573 | QLLEPFDKWDGKDLE | acetylation | [1] | 577 | PFDKWDGKDLEDLQI | acetylation | [1] | 605 | SAAGPWLKFRGHLDN | acetylation | [1] | 628 | AINIENGKANSVRNA | acetylation | [1] | 652 | DTARYYKKHGIRWVV | acetylation | [1] | 689 | GGRAIITKSFARIHE | acetylation | [1] | 700 | RIHETNLKKQGLLPL | acetylation | [1] | 717 | ADPSDYNKIHPVDKL | acetylation | [1] | 723 | NKIHPVDKLTIQGLK | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes the isomerization of citrate to isocitrate via cis-aconitate (By similarity). |
Sequence Annotation | REGION 192 194 Substrate binding (By similarity). REGION 670 671 Substrate binding (By similarity). METAL 385 385 Iron-sulfur (4Fe-4S) (By similarity). METAL 448 448 Iron-sulfur (4Fe-4S) (By similarity). METAL 451 451 Iron-sulfur (4Fe-4S) (By similarity). BINDING 99 99 Substrate (By similarity). BINDING 474 474 Substrate (By similarity). BINDING 479 479 Substrate (By similarity). BINDING 607 607 Substrate (By similarity). MOD_RES 28 28 Pyrrolidone carboxylic acid (By MOD_RES 50 50 N6-acetyllysine (By similarity). MOD_RES 559 559 Phosphoserine (By similarity). MOD_RES 573 573 N6-acetyllysine (By similarity). MOD_RES 605 605 N6-acetyllysine (By similarity). CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly) |
Keyword | 4Fe-4S; Acetylation; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Isopeptide bond; Lyase; Metal-binding; Mitochondrion; Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Transit peptide; Tricarboxylic acid cycle; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 780 AA |
Protein Sequence | MAPYSLLVTR LQKALGVRQY HVASALCQRA KVAMSHFEPS EYIRYDLLEK NINIVRKRLN 60 RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV 120 PSTIHCDHLI EAQLGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWRPGS GIIHQIILEN 180 YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGTLSG 240 WTSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN 300 HRMKKYLSKT GRADIANLAE EFKDHLVPDP GCQYDQVIEI NLNELKPHIN GPFTPDLAHP 360 VADVGTVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS 420 EQIRATIERD GYAQILRDVG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN 480 DANPETHAFV TSPEIVTALA IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRSDFDPG 540 QDTYQHPPKD SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA 600 GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI 660 GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPSDYNKIHP 720 VDKLTIQGLK DFAPGKPLNC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ 780 |
Gene Ontology | GO:0005739; C:mitochondrion; IDA:RGD. GO:0005634; C:nucleus; IEA:Compara. GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:RGD. GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:RGD. GO:0003994; F:aconitate hydratase activity; IDA:RGD. GO:0052632; F:citrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC. GO:0005506; F:iron ion binding; IEA:Compara. GO:0052633; F:isocitrate hydro-lyase (cis-aconitate-forming) activity; IEA:EC. GO:0006101; P:citrate metabolic process; IDA:RGD. GO:0006102; P:isocitrate metabolic process; IDA:RGD. GO:0006099; P:tricarboxylic acid cycle; IDA:RGD. |
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